TY - JOUR
AU - Xiong, Guangquan
AB - INTRODUCTIONThere is an increasing interest on a better comprehension of the interactions between flavor compounds and non‐volatile food components. Furthermore, the concentration of free volatile compounds in the gas phase depends on factors such as physicochemical properties and their interactions with other food constituents (Guichard, ).Myosin constitute the major myofibrillar proteins in meat. Myosin (43% of the total myofibrillar meat protein) is the major component of thick filaments which contains about 300 myosin molecules per filament. The myosin is not only important in muscle due to their role on contraction (Wang & Arntfield, ) but also for their importance on the functional properties in meat products such as water‐holding, emulsifying capacity, binding ability, and gelation (Arora & Damodaran, ; Reineccius, ).It has been reported that proteins can contribute to flavor release (Suppavorasatit, Lee, & Cadwallader, ) due to their ability to bind volatile compounds. Binding which is defined as a molecular bond existing between an aroma compound and a protein, is affected by several factors such as protein nature (Adams, Mottram, Parker, & Brown, ; Jouenne & Crouzet, ; Wang & Arntfield, ), ionic strength of the medium (Guichard, ; Perez‐Juan, Flores, & Toldra, 2007a), temperature (Seuvre, Turci, & 
TI - Effects of different salts and temperature on the binding force between the myosin and the volatile compounds of silver carp (Hypophthalmichthysmolitrix)
JF - Journal of Food Processing and Preservation
DO - 10.1111/jfpp.13267
DA - 2017-01-01
UR - https://www.deepdyve.com/lp/wiley/effects-of-different-salts-and-temperature-on-the-binding-force-rjZrOS53xw
SP - n/a
EP - n/a
VL - 41
IS - 6
DP - DeepDyve
ER -